Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20333 (TNR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 1B
Alternative name(s):
Tumor necrosis factor receptor 2
Short name=TNF-R2
Tumor necrosis factor receptor type II
Short name=TNF-RII
Short name=TNFR-II
p75
p80 TNF-alpha receptor
CD_antigen=CD120b
INN=Etanercept
Gene names
Name:TNFRSF1B
Synonyms:TNFBR, TNFR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity. Ref.4 Ref.19

Subunit structure

Binds to TRAF2. Interacts with BMX. Ref.18 Ref.19

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.4.

Isoform 2: Secreted Ref.4.

Tumor necrosis factor-binding protein 2: Secreted Ref.4.

Post-translational modification

Phosphorylated; mainly on serine residues and with a very low level on threonine residues.

A soluble form (tumor necrosis factor binding protein 2) is produced from the membrane form by proteolytic processing.

Pharmaceutical use

Available under the name Enbrel (Immunex and Wyeth-Ayerst). Used to treat moderate to severe rheumatoid arthritis (RA). Enbrel consist of the extracellular ligand-binding portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds to TNF-alpha and blocks its interactions with receptors.

Sequence similarities

Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processRNA destabilization

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from mutant phenotype PubMed 22480688. Source: BHF-UCL

immune response

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of membrane protein ectodomain proteolysis

Inferred from mutant phenotype PubMed 22480688. Source: BHF-UCL

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from direct assay PubMed 17010968. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

varicosity

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiontumor necrosis factor-activated receptor activity

Traceable author statement PubMed 8702885. Source: ProtInc

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20333-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20333-2)

Also known as: DS-TNFR2(Delta7,8); sTNFR2;

The sequence of this isoform differs from the canonical sequence as follows:
     263-268: GLIVGV → ASLACR
     269-461: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.11
Chain23 – 461439Tumor necrosis factor receptor superfamily member 1b, membrane form
PRO_0000034548
Chain27 – ?Tumor necrosis factor-binding protein 2PRO_0000034549

Regions

Topological domain23 – 257235Extracellular Potential
Transmembrane258 – 28730Helical; Potential
Topological domain288 – 461174Cytoplasmic Potential
Repeat39 – 7638TNFR-Cys 1
Repeat77 – 11842TNFR-Cys 2
Repeat119 – 16244TNFR-Cys 3
Repeat163 – 20139TNFR-Cys 4

Amino acid modifications

Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 53 By similarity
Disulfide bond54 ↔ 67 By similarity
Disulfide bond57 ↔ 75 By similarity
Disulfide bond78 ↔ 93 By similarity
Disulfide bond96 ↔ 110 By similarity
Disulfide bond100 ↔ 118 By similarity
Disulfide bond120 ↔ 126 By similarity
Disulfide bond134 ↔ 143 By similarity
Disulfide bond137 ↔ 161 By similarity
Disulfide bond164 ↔ 179 By similarity

Natural variations

Alternative sequence263 – 2686GLIVGV → ASLACR in isoform 2.
VSP_011826
Alternative sequence269 – 461193Missing in isoform 2.
VSP_011827
Natural variant1871V → M. Ref.6
Corresponds to variant rs2228494 [ dbSNP | Ensembl ].
VAR_017176
Natural variant1961M → R Frequent polymorphism; seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus. Ref.1 Ref.6 Ref.7 Ref.15 Ref.16 Ref.21 Ref.22
Corresponds to variant rs1061622 [ dbSNP | Ensembl ].
VAR_015434
Natural variant2321E → K. Ref.6 Ref.7 Ref.16 Ref.21
Corresponds to variant rs5746026 [ dbSNP | Ensembl ].
VAR_015435
Natural variant2361A → T. Ref.6
Corresponds to variant rs5746027 [ dbSNP | Ensembl ].
VAR_017177
Natural variant2641L → P. Ref.6
Corresponds to variant rs2229700 [ dbSNP | Ensembl ].
VAR_017178
Natural variant2691T → P. Ref.7
Corresponds to variant rs17879042 [ dbSNP | Ensembl ].
VAR_017179
Natural variant2951Q → R. Ref.6
Corresponds to variant rs5746032 [ dbSNP | Ensembl ].
VAR_017180
Natural variant3011P → R. Ref.7
Corresponds to variant rs17883432 [ dbSNP | Ensembl ].
VAR_017181

Experimental info

Sequence conflict35 – 373EPG → APT AA sequence Ref.12
Sequence conflict981S → P in AAN72434. Ref.4
Sequence conflict1021S → P in AAN72434. Ref.4
Sequence conflict1411R → P in AAA63262. Ref.15
Sequence conflict3631A → T in AAA63262. Ref.15

Secondary structure

............................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 27, 2002. Version 3.
Checksum: 603D0AE1CD69ACBF

FASTA46148,291
        10         20         30         40         50         60 
MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA QMCCSKCSPG 

        70         80         90        100        110        120 
QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC SSDQVETQAC TREQNRICTC 

       130        140        150        160        170        180 
RPGWYCALSK QEGCRLCAPL RKCRPGFGVA RPGTETSDVV CKPCAPGTFS NTTSSTDICR 

       190        200        210        220        230        240 
PHQICNVVAI PGNASMDAVC TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS 

       250        260        270        280        290        300 
FLLPMGPSPP AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV 

       310        320        330        340        350        360 
PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA PGVEASGAGE 

       370        380        390        400        410        420 
ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ ASSTMGDTDS SPSESPKDEQ 

       430        440        450        460 
VPFSKEECAF RSQLETPETL LGSTEEKPLP LGVPDAGMKP S 

« Hide

Isoform 2 (DS-TNFR2(Delta7,8)) (sTNFR2) [UniParc].

Checksum: 51A97BA5222FA444
Show »

FASTA26828,461

References

« Hide 'large scale' references
[1]"A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor."
Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K., Squires C.H., Thompson R.C., Vannice J.L.
Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-196.
[2]"A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins."
Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R., Dower S.K., Cosman D., Goodwin R.G.
Science 248:1019-1023(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Physical mapping and genomic structure of the human TNFR2 gene."
Beltinger C.P., White P.S., Maris J.M., Sulman E.P., Jensen S.J., Lepaslier D., Stallard B.J., Goeddel D.V., Desauvage F.J., Brodeur G.M.
Genomics 35:94-100(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Identification and characterization of a novel spliced variant that encodes human soluble tumor necrosis factor receptor 2."
Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D., Ricart W., Engel P.
Int. Immunol. 16:169-177(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION (ISOFORM 2).
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]NIEHS SNPs program
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-187; ARG-196; LYS-232; THR-236; PRO-264 AND ARG-295.
[7]SeattleSNPs variation discovery resource
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-196; LYS-232; PRO-269 AND ARG-301.
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: PNS.
[11]"Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells."
Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W., Brockhaus M.
J. Biol. Chem. 265:20131-20138(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
[12]"Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis."
Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.
Nephron 66:386-390(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-37.
Tissue: Urine.
[13]"Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors."
Engelmann H., Novick D., Wallach D.
J. Biol. Chem. 265:1531-1536(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-31.
Tissue: Urine.
[14]"Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences."
Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R., Brockhaus M., Lesslauer W.
Cytokine 2:231-237(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
[15]"Complementary DNA cloning of a receptor for tumor necrosis factor and demonstration of a shed form of the receptor."
Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D., Ringold G.M.
Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT ARG-196.
[16]"New single nucleotide polymorphisms in the coding region of human TNFR2: association with systemic lupus erythematosus."
Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.
Genes Immun. 1:501-503(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, VARIANTS ARG-196 AND LYS-232.
[17]"Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation."
Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M., Lipari M.T., Goeddel D.V.
J. Biol. Chem. 267:21172-21178(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[18]"A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor."
Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.
Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF2.
[19]"Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role in endothelial cell migration and angiogenesis."
Pan S., An P., Zhang R., He X., Yin G., Min W.
Mol. Cell. Biol. 22:7512-7523(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMX.
[20]"Structural basis for self-association and receptor recognition of human TRAF2."
Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.
Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH TRAF2.
[21]"Association of tumor necrosis factor receptor type II polymorphism 196R with systemic lupus erythematosus in the Japanese: molecular and functional analysis."
Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y., Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.
Arthritis Rheum. 44:2819-2827(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-196 AND LYS-232.
[22]"Comment: the methionine 196 arginine polymorphism in exon 6 of the TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary syndrome and hyperandrogenism."
Peral B., San Millan J.L., Castello R., Moghetti P., Escobar-Morreale H.F.
J. Clin. Endocrinol. Metab. 87:3977-3983(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-196.
+Additional computationally mapped references.

Web resources

SeattleSNPs
NIEHS-SNPs
Enbrel

Clinical information on Enbrel

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55994 mRNA. Translation: AAA36755.1.
M32315 mRNA. Translation: AAA59929.1.
U52165 expand/collapse EMBL AC list , U52156, U52157, U52158, U52159, U52160, U52161, U52162, U52163, U52164 Genomic DNA. Translation: AAC50622.1.
AY148473 mRNA. Translation: AAN72434.1.
BT019927 mRNA. Translation: AAV38730.1.
AY264804 Genomic DNA. Translation: AAO89076.1.
AY342040 Genomic DNA. Translation: AAP88939.1.
AL031276, AL357835 Genomic DNA. Translation: CAI19225.1.
AL357835, AL031276 Genomic DNA. Translation: CAH73721.1.
CH471130 Genomic DNA. Translation: EAW71733.1.
BC052977 mRNA. Translation: AAH52977.1.
S63368 mRNA. Translation: AAB19824.2.
M35857 mRNA. Translation: AAA63262.1.
AB030950 Genomic DNA. Translation: BAA89053.1.
PIRA35356.
RefSeqNP_001057.1. NM_001066.2.
UniGeneHs.256278.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA9X-ray2.30G/H420-428[»]
3ALQX-ray3.00R/S/T/U/V/W33-205[»]
ProteinModelPortalP20333.
SMRP20333. Positions 37-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112987. 26 interactions.
DIPDIP-78N.
IntActP20333. 12 interactions.
MINTMINT-134958.
STRING9606.ENSP00000365435.

Chemistry

ChEMBLCHEMBL1250356.
DrugBankDB00005. Etanercept.
DB00065. Infliximab.
GuidetoPHARMACOLOGY1871.

PTM databases

PhosphoSiteP20333.

Polymorphism databases

DMDM21264534.

Proteomic databases

PaxDbP20333.
PeptideAtlasP20333.
PRIDEP20333.

Protocols and materials databases

DNASU7133.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376259; ENSP00000365435; ENSG00000028137. [P20333-1]
GeneID7133.
KEGGhsa:7133.
UCSCuc001att.3. human. [P20333-1]

Organism-specific databases

CTD7133.
GeneCardsGC01P012161.
HGNCHGNC:11917. TNFRSF1B.
HPACAB013045.
HPA004796.
MIM191191. gene.
neXtProtNX_P20333.
PharmGKBPA36610.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42764.
HOGENOMHOG000132845.
HOVERGENHBG054237.
InParanoidP20333.
KOK05141.
OMAGNASMDA.
OrthoDBEOG786H2Q.
PhylomeDBP20333.
TreeFamTF331157.

Gene expression databases

ArrayExpressP20333.
BgeeP20333.
CleanExHS_TNFRSF1B.
GenevestigatorP20333.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020411. TNFR_1B.
[Graphical view]
PfamPF00020. TNFR_c6. 2 hits.
[Graphical view]
PRINTSPR01919. TNFACTORR1B.
SMARTSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20333.
GeneWikiTNFRSF1B.
GenomeRNAi7133.
NextBio27909.
PMAP-CutDBP20333.
PROP20333.
SOURCESearch...

Entry information

Entry nameTNR1B_HUMAN
AccessionPrimary (citable) accession number: P20333
Secondary accession number(s): B1AJZ3 expand/collapse secondary AC list , Q16042, Q6YI29, Q9UIH1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries